C
Christopher P. Walczak
Researcher at Stanford University
Publications - 14
Citations - 495
Christopher P. Walczak is an academic researcher from Stanford University. The author has contributed to research in topics: Endoplasmic reticulum & Endoplasmic-reticulum-associated protein degradation. The author has an hindex of 8, co-authored 14 publications receiving 374 citations. Previous affiliations of Christopher P. Walczak include University of Michigan & Central Michigan University.
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Journal ArticleDOI
Ribosomal protein RPL26 is the principal target of UFMylation.
Christopher P. Walczak,Dara Leto,Lichao Zhang,Celeste Riepe,Ryan Muller,Paul A. DaRosa,Nicholas T. Ingolia,Joshua E. Elias,Ron R. Kopito +8 more
TL;DR: Biochemical analysis and structural modeling establish that UFMylation is a ribosomal modification specialized to facilitate metazoan-specific protein biogenesis at the ER, suggesting that this modification plays a direct role in cotranslational protein translocation into the ER.
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A PDI Family Network Acts Distinctly and Coordinately with ERp29 To Facilitate Polyomavirus Infection
TL;DR: How a PDI family functions coordinately and distinctly to promote Py infection is revealed and a role of viral cysteines in this process is pinpoints.
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Genome-wide CRISPR Analysis Identifies Substrate-Specific Conjugation Modules in ER-Associated Degradation.
Dara Leto,David W. Morgens,Lichao Zhang,Christopher P. Walczak,Joshua E. Elias,Michael C. Bassik,Ron R. Kopito +6 more
TL;DR: These findings demonstrate that parallel CRISPR analysis can be used to deconvolve highly complex cell biological processes and identify new biochemical pathways in protein quality control.
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A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum.
TL;DR: A novel role for a cytosolic chaperone in the membrane penetration of a nonenveloped virus is identified and the possibility that the SV40-induced foci represent cytosol entry sites is raised.
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High-Throughput Screen for Escherichia coli Heat Shock Protein 70 (Hsp70/DnaK): ATPase Assay in Low Volume by Exploiting Energy Transfer
Yoshinari Miyata,Lyra Chang,Anthony J. Bainor,Thomas J. McQuade,Christopher P. Walczak,Yaru Zhang,Martha J. Larsen,Paul D. Kirchhoff,Jason E. Gestwicki +8 more
TL;DR: An energy transfer strategy that was originally reported by Zuck et al. is adopted, and this simple and inexpensive adaptation of a colorimetric method might be suitable for screening against Hsp70 family members.